Physicochemical forces which sequester cell solutes from soluble form to organized structures are investigated with regard to molecular conformations of components and interacting species. Earlier results showed that ordered, negative charges (glycosaminoglycans and acidic polysaccharides) have specific ordering effects on amine cations; exhibit conformation-promoting effects on otherwise nonordered cationic polypeptides; on poly L-lysine, all with sufficient anionic density promote a non-specific high degree of alpha-helical conformation. Specificity due to peptide structure revealed that heparin (and other polyanions) with poly L-lysine:L-tyrosine promotes beta-protein structure, while with poly L-lysine:L-phenylalanine induces alpha-helical order. That the nature of conformational change in protein models due to interaction with heparin depends upon constellations of amino acids and their proclivity for alpha-helix or beta-structures is significant in the molecular basis of multianion action in granule formation and enzyme activation. Currently, a molecular basis for heparin regulation of tyrosine hydroxylase activity, heparin in isoelectric focusing, and heparin fractionation and fractions have been studied on the basis of these molecular characterizations.